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- W2094906141 abstract "Penicillin G acylase (PGA) is a heterodimeric enzyme synthesized as a single-polypeptide precursor that undergoes an autocatalytic processing to remove an internal spacer peptide to produce the active enzyme. We constructed a single-chain PGA not dependent on autoproteolytic processing. The mature sequence of the beta-domain was expressed as the N terminus of a new polypeptide, connected by a random tetra-peptide to the alpha-domain, to afford a permuted protein. We found several active enzymes among variants differing in their linker peptides. Protein expression analysis showed that the functional single-chain variants were produced when using a Sec-dependent leader peptide, or when expressed inside the bacterial cytoplasm. Active-site titration experiments showed that the single-chain proteins displayed similar k(cat) values to the ones obtained with the wild-type enzyme. Interestingly, the single-chain proteins also displayed close to 100% of functional active sites compared to 40% to 70% functional yield usually obtained with the heterodimeric protein." @default.
- W2094906141 created "2016-06-24" @default.
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- W2094906141 date "2004-06-01" @default.
- W2094906141 modified "2023-10-18" @default.
- W2094906141 title "Production of a fully functional, permuted single-chain penicillin G acylase" @default.
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- W2094906141 doi "https://doi.org/10.1110/ps.03436604" @default.
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